ABSTRACT The recent outbreak of pneumonia-causing COVID-19 in China is an urgent global public health issue with an increase in mortality and morbidity. Here we report our modelled homo-trimer structure of COVID-19 spike glycoprotein in both closed (ligand-free) and open (ligand-bound) conformation, which is involved in host cell adhesion. We also predict the unique N- and O-linked glycosylation sites of spike glycoprotein that distinguish it from the SARS and underlines shielding and camouflage of COVID-19 from the host the defence system. Furthermore, our study also highlights the key finding that the S1 domain of COVID-19 spike glycoprotein potentially interacts with the human CD26, a key immunoregulatory factor for hijacking and virulence. These findings accentuate the unique features of COVID-19 and assist in the development of new therapeutics.
【저자키워드】 coronavirus, glycosylation, spike glycoprotein, docking, DPP4, CD26, 【초록키워드】 COVID-19, Mortality, China, outbreak, morbidity, virulence, predict, host cell, shielding, global public health, S1 domain, Host, feature, highlight, glycosylation site, involved, unique, interact, increase in, assist, ligand-bound, 【제목키워드】 COVID-19, Interaction,